Experiments are now in progress to determine conditions under which glucose, mannose and N-acetyl glucosamine are transferred from their nucleoside diphosphate coenzyme form to phosphorylated dolichol. The aim of this work is to determine the conditions which will allow us to obtain reproducible data so that we will be able to compare glycolipid metabolism in normal tissue and tissue from animals with diseases such as diabetes. In addition to these studies we are continuing our attempts to purify a polyprenyl phosphate phosphatase which was found in T. pyriformis. Theis enzyme has been partially characterized and should be a useful tool in studies which we are conducting aimed at characterizing the dolichols which are linked to sugars. No data has been reported to indicate whether different sugars are linekd to the same or different dolichols. The dolichyl phosphate hydrolyzing enzyme is also of interest because it may function to control the level of dolichyl phosphate and thus the rate of glycoprotein synthesis. Experiments designed to test possible changes in the level of activity of this enzyme are planned.